ID W1UDT0_CLOBU Unreviewed; 481 AA.
AC W1UDT0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN ORFNames=Q607_CBUC00021G0082 {ECO:0000313|EMBL:ETI91640.1};
OS Clostridium butyricum DORA_1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1403941 {ECO:0000313|EMBL:ETI91640.1, ECO:0000313|Proteomes:UP000018876};
RN [1] {ECO:0000313|EMBL:ETI91640.1, ECO:0000313|Proteomes:UP000018876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DORA_1 {ECO:0000313|Proteomes:UP000018876};
RA Brown C.T., Sharon I., Thomas B.C., Castelle C.J., Morowitz M.J.,
RA Banfield J.F.;
RT "A Varibaculum cambriense genome reconstructed from a premature infant gut
RT community with otherwise low bacterial novelty that shifts toward anaerobic
RT metabolism during the third week of life.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an
CC N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA-
CC COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72;
CC Evidence={ECO:0000256|ARBA:ARBA00001279};
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00006594}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETI91640.1}.
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DR EMBL; AZLX01000021; ETI91640.1; -; Genomic_DNA.
DR AlphaFoldDB; W1UDT0; -.
DR PATRIC; fig|1403941.3.peg.354; -.
DR Proteomes; UP000018876; Unassembled WGS sequence.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR011639; MethylTrfase_TaqI-like_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR33841:SF6; DNA METHYLTRANSFERASE A; 1.
DR PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR Pfam; PF07669; Eco57I; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:ETI91640.1};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 99..206
FT /note="Type II methyltransferase M.TaqI-like"
FT /evidence="ECO:0000259|Pfam:PF07669"
SQ SEQUENCE 481 AA; 56172 MW; A628C28046679EB5 CRC64;
MAGILETKKE YLKILDPGAG SGILSAALIS KLQNTNVKSI DLTLYENDNN ILPLLHKNIE
YMTKTSSIII NYSIIEKNYI LDNKDDFNST LLAHKDLCKY DFIICNPPYL KISKDAPEAK
AMPLVCYGAP NMYFLFMSMA LFELKENSQM VFIIPRSWTF GAYFKKFREY LLLEARIKHI
HLFVSRNKVF EKEKVLQETI IVHIVKTKEK LDLIEISSTE SNFDFKDINS FMVPYNLAVS
EDENKFVYLP INKEEVEILN KINKFKYTLQ EIGIRLKTGL TVSFRNRGLL HDKADKENVP
LIYSTHFKNG TIEFPIQTDK KQYIDNLKKG LVQKNKDYLF IKRFTSKEEK RRIQPAIYLK
NICNKYDYIS TDNKINFIDT IDKNEILTKD EIYGLYIVFN STLYDKYYRI LNGSTQVNAT
EINYMHVPNR KQLKEIGKRI QDINDLSVKT CDEILEELLD GEVRRCKRDI EIIRNAKSSA
I
//
